ID T0Q5B0_SAPDV Unreviewed; 594 AA.
AC T0Q5B0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU366014};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU366014};
GN ORFNames=SDRG_09530 {ECO:0000313|EMBL:EQC33009.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC33009.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC33009.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC33009.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase that functions in several pathways of DNA
CC repair. Involved in base excision repair (BER) responsible for repair
CC of lesions that give rise to abasic (AP) sites in DNA. Also contributes
CC to DNA double-strand break repair by non-homologous end joining and
CC homologous recombination. Has both template-dependent and template-
CC independent (terminal transferase) DNA polymerase activities. Has also
CC a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
CC {ECO:0000256|RuleBase:RU366014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|RuleBase:RU366014};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU366014}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC {ECO:0000256|ARBA:ARBA00008323, ECO:0000256|RuleBase:RU366014}.
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DR EMBL; JH767161; EQC33009.1; -; Genomic_DNA.
DR RefSeq; XP_008613695.1; XM_008615473.1.
DR AlphaFoldDB; T0Q5B0; -.
DR EnsemblProtists; EQC33009; EQC33009; SDRG_09530.
DR GeneID; 19950257; -.
DR VEuPathDB; FungiDB:SDRG_09530; -.
DR OrthoDB; 49764at2759; -.
DR Proteomes; UP000030762; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR019843; DNA_pol-X_BS.
DR InterPro; IPR028207; DNA_pol_B_palm_palm.
DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR002008; DNA_pol_X_beta-like.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR PANTHER; PTHR11276:SF43; DNA POLYMERASE IV; 1.
DR PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR Pfam; PF14792; DNA_pol_B_palm; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF10391; DNA_pol_lambd_f; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00870; DNAPOLXBETA.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81585; PsbU/PolX domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|RuleBase:RU366014};
KW DNA repair {ECO:0000256|RuleBase:RU366014};
KW DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU366014};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU366014}; Nucleus {ECO:0000256|RuleBase:RU366014};
KW Reference proteome {ECO:0000313|Proteomes:UP000030762};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366014}.
FT DOMAIN 68..167
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 22..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 326
FT /note="Nucleophile; Schiff-base intermediate with DNA; for
FT 5'-dRP lyase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR622312-50"
SQ SEQUENCE 594 AA; 66025 MW; 90A893DB01C5C247 CRC64;
MLSAKRKARF FDKLNEIYVP TKRPAPETDA PPVLASSAGD ASDRRQSFPP MAVTKALVDK
AHRRQSVPLA GPLQGLRLLI VALGSDMSRR RLDIWTTQVA KAGGQLVTTC DDSENTIVVA
SLSLSRERLC SYCHVPELSP SLRVVSPDWL VYVIQHRTLP PDGMFAWTDV APTTAPTEDA
PPQRAFYESS PSNTQESPAP LPTAQSAIAS GSPLRALDED MAYRKRVFYE INPSMVVVHA
EEAADPRQIK ATSFVCATTS VQSINHNAHL TSVLDELIEY LAVEKDEWRE NSYKRMVSIL
KQLPAKVTST AALRPQYGLN ATGIAKIREI LETGTLRKLE AKKADARLQV LRTFANIWGV
GPSTATSLYS QGFRSLDALR MRQDEVLNPQ QRIGLEHYAD FLVKIPRAEV EDIQAIVKAT
VAMIHPTAVS VTCGSYRRGK LQSGDVDILI TDPLADECVL LPDLLRELHK RAFLTDDLTT
VTEHHIGGCD SYMGVCRVDE SRPFRRIDLK VYPRHLFGFA QLYFTGSDHF NRSMRAFAKQ
KGYSLTDRGL TKVARAKGAK KLKQAPGLIC PDEKDVFIAL QLPYKRPEER NCMA
//
